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Protein

Metal-response element-binding transcription factor 2

Gene

Mtf2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Polycomb group (PcG) that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex. Acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting the PRC2 complex, leading to enhance PRC2 H3K27me3 methylation activity. Regulates the transcriptional networks during embryonic stem cell self-renewal and differentiation. Promotes recruitment of the PRC2 complex to the inactive X chromosome in differentiating XX ES cells and PRC2 recruitment to target genes in undifferentiated ES cells. Required to repress Hox genes by enhancing H3K27me3 methylation of the PRC2 complex. In some conditions may act as an inhibitor of PRC2 activity: able to activate the CDKN2A gene and promote cellular senescence by suppressing the catalytic activity of the PRC2 complex locally. Binds to the metal-regulating-element (MRE) of MT1A gene promoter.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri102 – 15756PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri201 – 25555PHD-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • methylated histone binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • chromatin modification Source: UniProtKB-KW
  • negative regulation of histone H3-K27 methylation Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of histone H3-K27 methylation Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • segment specification Source: UniProtKB
  • stem cell differentiation Source: UniProtKB
  • stem cell population maintenance Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-212300. PRC2 methylates histones and DNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Metal-response element-binding transcription factor 2
Alternative name(s):
Metal regulatory transcription factor 2
Metal-response element DNA-binding protein M96
Polycomb-like protein 2
Short name:
mPCl2
Zinc-regulated factor 1
Short name:
ZiRF1
Gene namesi
Name:Mtf2
Synonyms:Pcl2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:105050. Mtf2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice survive to birth; however, most of them die before weaning. Axial skeletal alterations that are characteristic of posterior transformations are observed: ectopic ribs that associate with the seventh cervical vertebra (C7) are frequently observed. Consistent with this malformation, sternums are shifted anteriorly. The odontoid process, which is normally a characteristic of the second cervical vertebra (C2), is frequently associated with the first cervical vertebra (C1).1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 593593Metal-response element-binding transcription factor 2PRO_0000059318Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ02395.
MaxQBiQ02395.
PaxDbiQ02395.
PRIDEiQ02395.

PTM databases

iPTMnetiQ02395.
PhosphoSiteiQ02395.

Expressioni

Gene expression databases

BgeeiQ02395.
ExpressionAtlasiQ02395. baseline and differential.
GenevisibleiQ02395. MM.

Interactioni

Subunit structurei

Associated component of the PRC2 complex.

Binary interactionsi

WithEntry#Exp.IntActNotes
EedQ921E63EBI-2531578,EBI-904301
Ezh1P703513EBI-2531578,EBI-2531737
Ezh2Q611884EBI-2531578,EBI-904311

GO - Molecular functioni

  • methylated histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi201592. 13 interactions.
DIPiDIP-56991N.
IntActiQ02395. 9 interactions.
STRINGi10090.ENSMUSP00000080278.

Structurei

Secondary structure

1
593
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi51 – 555Combined sources
Beta strandi61 – 7010Combined sources
Turni71 – 744Combined sources
Beta strandi75 – 806Combined sources
Turni81 – 833Combined sources
Beta strandi84 – 896Combined sources
Turni90 – 923Combined sources
Beta strandi105 – 1084Combined sources
Beta strandi119 – 1213Combined sources
Beta strandi123 – 1253Combined sources
Beta strandi128 – 1303Combined sources
Turni131 – 1333Combined sources
Beta strandi134 – 1363Combined sources
Helixi140 – 1445Combined sources
Helixi152 – 1565Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EQJNMR-A40-98[»]
2YT5NMR-A104-162[»]
ProteinModelPortaliQ02395.
SMRiQ02395. Positions 36-162, 202-253.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02395.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 10158TudorAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi338 – 3414Poly-Lys
Compositional biasi497 – 5026Poly-Arg

Domaini

The Tudor domain recognizes and binds H3K36me3.1 Publication

Sequence similaritiesi

Belongs to the Polycomblike family.Curated
Contains 2 PHD-type zinc fingers.PROSITE-ProRule annotation
Contains 1 Tudor domain.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri102 – 15756PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri201 – 25555PHD-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG4323. Eukaryota.
ENOG410XQ6E. LUCA.
GeneTreeiENSGT00390000009222.
HOGENOMiHOG000010307.
HOVERGENiHBG004755.
InParanoidiQ02395.
KOiK11485.
OMAiSDDKWLC.
OrthoDBiEOG73V6JJ.
PhylomeDBiQ02395.
TreeFamiTF106420.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
InterProiIPR025894. Mtf2_C_dom.
IPR002999. Tudor.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF14061. Mtf2_C. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00249. PHD. 2 hits.
SM00333. TUDOR. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 2 hits.
PROSITEiPS01359. ZF_PHD_1. 2 hits.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q02395-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRDSTGAGNS LVHKRSPLRR NQKTSASLNK LSLQDGHKAK KPACKFEEGQ
60 70 80 90 100
DVLARWSDGL FYLGTIKKIN ILKQSCFIIF EDSSKSWVLW KDIQTGATGS
110 120 130 140 150
GEMVCTICQE EYSEAPNEMV ICDKCGQGYH QLCHTPHIDS SVIDSDEKWL
160 170 180 190 200
CRQCVFATTT KRGGALKKGP NAKALQVMKQ TLPYSVADLE WDAGHKTNVQ
210 220 230 240 250
QCYCYCGGPG DWYLKMLQCC KCKQWFHEAC VQCLQKPMLF GDRFYTFICS
260 270 280 290 300
VCSSGPEYLK RLPLQWVDIA HLCLYNLSVI HKKKYFDSEL ELMTYINENW
310 320 330 340 350
DRLHPGELAD TPKSERYEHV LEALNDYKTM FMSGKEIKKK KHLFGLRIRV
360 370 380 390 400
PPVPPNVAFK AEKEPEGTSH EFKIKGRKAS KPTSDSREVS NGIEKKGKKK
410 420 430 440 450
SVGRPPGPYT RKMIQKTAEL PLDKESVSEN PTLDLPCSIG RTEGIAHSSN
460 470 480 490 500
TSDVDLTGAS SANETTSASI SRHCGLSDSR KRTRTGRSWP AAIPHLRRRR
510 520 530 540 550
GRLPRRALQT QNSEVVKDDE GKEDYQFEEL NTEILNNLAD QELQLNHLKN
560 570 580 590
SITSYFGAAG RIACGEKYRV LARRVTLDGK VQYLVEWEGA TAS
Length:593
Mass (Da):66,924
Last modified:November 22, 2005 - v2
Checksum:iC595438196DC3E0F
GO
Isoform 2 (identifier: Q02395-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-102: Missing.

Show »
Length:491
Mass (Da):55,586
Checksum:i7FBA64012D15553F
GO

Sequence cautioni

The sequence AAH24889.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH29076.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti200 – 2012QQ → PE in AAC34714 (PubMed:7772254).Curated
Sequence conflicti282 – 2821Missing in AAC34714 (PubMed:7772254).Curated
Sequence conflicti394 – 3941E → K in AAH57163 (PubMed:15489334).Curated
Sequence conflicti397 – 3971G → K in AAH57163 (PubMed:15489334).Curated
Sequence conflicti519 – 5191D → G in BAC28027 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 102102Missing in isoform 2. 3 PublicationsVSP_016240Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK032798 mRNA. Translation: BAC28027.1.
AK032819 mRNA. Translation: BAC28039.1.
AK031409 mRNA. Translation: BAC27390.1.
AK139685 mRNA. Translation: BAE24103.1.
BC057163 mRNA. Translation: AAH57163.1.
BC092237 mRNA. Translation: AAH92237.1.
BC100340 mRNA. Translation: AAI00341.1.
BC024889 mRNA. Translation: AAH24889.1. Sequence problems.
BC029076 mRNA. Translation: AAH29076.1. Sequence problems.
S78454 mRNA. Translation: AAC34714.1.
CCDSiCCDS39201.1. [Q02395-1]
RefSeqiNP_001240806.1. NM_001253877.1. [Q02395-2]
NP_001240807.1. NM_001253878.1. [Q02395-2]
NP_001240808.1. NM_001253879.1. [Q02395-2]
NP_001240809.1. NM_001253880.1. [Q02395-2]
NP_038855.2. NM_013827.3. [Q02395-1]
XP_006534874.1. XM_006534811.2. [Q02395-2]
XP_011247715.1. XM_011249413.1. [Q02395-2]
XP_011247716.1. XM_011249414.1. [Q02395-2]
XP_011247717.1. XM_011249415.1. [Q02395-2]
XP_011247718.1. XM_011249416.1. [Q02395-2]
UniGeneiMm.257149.

Genome annotation databases

EnsembliENSMUST00000081567; ENSMUSP00000080278; ENSMUSG00000029267. [Q02395-1]
GeneIDi17765.
KEGGimmu:17765.
UCSCiuc008ynj.2. mouse. [Q02395-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK032798 mRNA. Translation: BAC28027.1.
AK032819 mRNA. Translation: BAC28039.1.
AK031409 mRNA. Translation: BAC27390.1.
AK139685 mRNA. Translation: BAE24103.1.
BC057163 mRNA. Translation: AAH57163.1.
BC092237 mRNA. Translation: AAH92237.1.
BC100340 mRNA. Translation: AAI00341.1.
BC024889 mRNA. Translation: AAH24889.1. Sequence problems.
BC029076 mRNA. Translation: AAH29076.1. Sequence problems.
S78454 mRNA. Translation: AAC34714.1.
CCDSiCCDS39201.1. [Q02395-1]
RefSeqiNP_001240806.1. NM_001253877.1. [Q02395-2]
NP_001240807.1. NM_001253878.1. [Q02395-2]
NP_001240808.1. NM_001253879.1. [Q02395-2]
NP_001240809.1. NM_001253880.1. [Q02395-2]
NP_038855.2. NM_013827.3. [Q02395-1]
XP_006534874.1. XM_006534811.2. [Q02395-2]
XP_011247715.1. XM_011249413.1. [Q02395-2]
XP_011247716.1. XM_011249414.1. [Q02395-2]
XP_011247717.1. XM_011249415.1. [Q02395-2]
XP_011247718.1. XM_011249416.1. [Q02395-2]
UniGeneiMm.257149.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EQJNMR-A40-98[»]
2YT5NMR-A104-162[»]
ProteinModelPortaliQ02395.
SMRiQ02395. Positions 36-162, 202-253.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201592. 13 interactions.
DIPiDIP-56991N.
IntActiQ02395. 9 interactions.
STRINGi10090.ENSMUSP00000080278.

PTM databases

iPTMnetiQ02395.
PhosphoSiteiQ02395.

Proteomic databases

EPDiQ02395.
MaxQBiQ02395.
PaxDbiQ02395.
PRIDEiQ02395.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000081567; ENSMUSP00000080278; ENSMUSG00000029267. [Q02395-1]
GeneIDi17765.
KEGGimmu:17765.
UCSCiuc008ynj.2. mouse. [Q02395-1]

Organism-specific databases

CTDi22823.
MGIiMGI:105050. Mtf2.

Phylogenomic databases

eggNOGiKOG4323. Eukaryota.
ENOG410XQ6E. LUCA.
GeneTreeiENSGT00390000009222.
HOGENOMiHOG000010307.
HOVERGENiHBG004755.
InParanoidiQ02395.
KOiK11485.
OMAiSDDKWLC.
OrthoDBiEOG73V6JJ.
PhylomeDBiQ02395.
TreeFamiTF106420.

Enzyme and pathway databases

ReactomeiR-MMU-212300. PRC2 methylates histones and DNA.

Miscellaneous databases

ChiTaRSiMtf2. mouse.
EvolutionaryTraceiQ02395.
PROiQ02395.
SOURCEiSearch...

Gene expression databases

BgeeiQ02395.
ExpressionAtlasiQ02395. baseline and differential.
GenevisibleiQ02395. MM.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
InterProiIPR025894. Mtf2_C_dom.
IPR002999. Tudor.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF14061. Mtf2_C. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00249. PHD. 2 hits.
SM00333. TUDOR. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 2 hits.
PROSITEiPS01359. ZF_PHD_1. 2 hits.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Egg, Testis and Wolffian duct.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and NMRI.
    Tissue: Head, Mammary tumor and Placenta.
  3. "Isolation of a cDNA encoding a metal response element binding protein using a novel expression cloning procedure: the one hybrid system."
    Inouye C., Remondelli P., Karin M., Elledge S.
    DNA Cell Biol. 13:731-742(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-476 (ISOFORM 2).
    Tissue: Lymphoma.
  4. "Interactions of the zinc-regulated factor (ZiRF1) with the mouse metallothionein Ia promoter."
    Remondelli P., Leone A.
    Biochem. J. 323:79-85(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Polycomb-like 2 associates with PRC2 and regulates transcriptional networks during mouse embryonic stem cell self-renewal and differentiation."
    Walker E., Chang W.Y., Hunkapiller J., Cagney G., Garcha K., Torchia J., Krogan N.J., Reiter J.F., Stanford W.L.
    Cell Stem Cell 6:153-166(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ASSOCIATION WITH THE PRC2 COMPLEX.
  6. "Polycomblike 2 facilitates the recruitment of PRC2 Polycomb group complexes to the inactive X chromosome and to target loci in embryonic stem cells."
    Casanova M., Preissner T., Cerase A., Poot R., Yamada D., Li X., Appanah R., Bezstarosti K., Demmers J., Koseki H., Brockdorff N.
    Development 138:1471-1482(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ASSOCIATION WITH THE PRC2 COMPLEX, SUBCELLULAR LOCATION.
  7. "Mammalian polycomb-like Pcl2/Mtf2 is a novel regulatory component of PRC2 that can differentially modulate polycomb activity both at the Hox gene cluster and at Cdkn2a genes."
    Li X., Isono K., Yamada D., Endo T.A., Endoh M., Shinga J., Mizutani-Koseki Y., Otte A.P., Casanova M., Kitamura H., Kamijo T., Sharif J., Ohara O., Toyada T., Bernstein B.E., Brockdorff N., Koseki H.
    Mol. Cell. Biol. 31:351-364(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  8. Cited for: H3K36ME3-BINDING.
  9. "Polycomb-like 3 promotes polycomb repressive complex 2 binding to CpG islands and embryonic stem cell self-renewal."
    Hunkapiller J., Shen Y., Diaz A., Cagney G., McCleary D., Ramalho-Santos M., Krogan N., Ren B., Song J.S., Reiter J.F.
    PLoS Genet. 8:E1002576-E1002576(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH THE PRC2 COMPLEX.
  10. "Solution structure of the tudor domain of metal-response element-binding transcription factor 2."
    RIKEN structural genomics initiative (RSGI)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 40-98 AND 104-162.

Entry informationi

Entry nameiMTF2_MOUSE
AccessioniPrimary (citable) accession number: Q02395
Secondary accession number(s): Q05C61
, Q569Z8, Q6PG89, Q8BGP9, Q8BSJ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 22, 2005
Last modified: June 8, 2016
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.